Solution structure of antifreeze glycopeptides. Determination of the major conformers of the glycosidic linkages

S. W. Homans, A. L. DeVries, S. B. Parker

Research output: Contribution to journalArticlepeer-review

Abstract

Using data obtained from 1H-1H correlated spectroscopy and one- and two-dimensional NOE measurements, we have determined the preferential solution conformation of the disaccharide unit Galβ(1-3)Gal-NAc in the antifreeze glycopeptide (Galß(l-3)GalNAcαl-Thr-Ala-Ala)n derived from the blood of the antarctic fish Trematomas borchgrevinki. The disaccharide, which is a rigid unit, exists with a restricted orientation about the GalNAc-αl-Thr linkage. Preliminary evidence indicates that the backbone (Ala-Ala-Thr)n lies in an extended helical conformation. Antifreeze glycopeptide 1H NMR Glycosidic linkage Dissaccharide structure Nuclear Overhauser effect.

Original languageEnglish (US)
Pages (from-to)133-137
Number of pages5
JournalFEBS Letters
Volume183
Issue number1
DOIs
StatePublished - Apr 8 1985

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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